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Literature summary for 6.1.1.B3 extracted from

  • Ray, S.; Banerjee, V.; Blaise, M.; Banerjee, B.; Das, K.P.; Kern, D.; Banerjee, R.
    Critical role of zinc ion on E. coli glutamyl-queuosine-tRNA(Asp) synthetase (Glu-Q-RS) structure and function (2014), Protein J., 33, 143-149 .
    View publication on PubMed
Search for more literature for 6.1.1.B3

Cloned(Commentary)

Cloned (Comment) Organism
gene gluQ, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Rosetta II Escherichia coli

Protein Variants

Protein Variants Comment Organism
C101S/C103S site-directed mutagenesis, in the mutant the zinc ion still remains coordinated but the variant becomes structurally labile and acquires aggregation capacity. The extent of aggregation of the protein is significantly decreased in presence of the small substrates and more particularly by adenosine triphosphate. Addition of zinc increases significantly the solubility of the variant. The aminoacylation assay reveals a decrease in activity of the mutant even after addition of zinc as compared to the wild-type, although the secondary structure of the protein is not altered. Unlike wild type Glu-Q-RS, the mutant shows a strong tendency to aggregate in solution at room temperature, addition of a saturating concentration of the small substrate ATP and/or L-Glu decreases the rate of aggregation of C101S/C103S Glu-Q-RS, ATP has the most efficient effect Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Zn2+ required, tetracoordinated to residues Cys101, Cys103, Cys119 and Tyr115. The zinc ion has a high impact on the enzyme structure and function. Enzyme Glu-Q-RS contain a single zinc-binding site in their putative tRNA acceptor stem-binding domain. Quantification by X-ray fluorescence spectrometry technique. Absence of saturating zinc in solution displays dramatic change in the solubility of the protein Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate + tRNAAsp Escherichia coli
-
 AMP + diphosphate + L-glutamyl-tRNAAsp
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P27305
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + tRNAAsp
-
 Escherichia coli AMP + diphosphate + L-glutamyl-tRNAAsp
-
 ?
additional information Glu-Q-RS glutamylates the Q34 residue of the anticodon of tRNAAsp, hence it is a tRNA hypermodifying enzyme Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More determination and comparisons of three-dimensional structures of free enzyme Glu-Q-RS and Glu-bound Glu-Q-RS Escherichia coli

Synonyms

Synonyms Comment Organism
Glu-Q-RS
-
 Escherichia coli
gluQ
-
 Escherichia coli
glutamyl-queuosine-tRNAAsp synthetase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
evolution glutamyl-QtRNA Asp synthetase (Glu-Q-RS) from Escherichia coli is a paralogue of glutamyl-tRNA synthetase, GluRS, both containing one zinc ion Escherichia coli
malfunction Absence of saturating zinc in solution displays dramatic change in the solubility of the protein Escherichia coli